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The DNase enzyme relies on the presence of a divalent cation, which is usually Ca 2+, for proper function. The active site of DNase I includes two histidine residues (His134 and His252) and two acidic residues (Glu78 and Asp 212), all of which are critical for the general acid-base catalysis of phosphodiester bonds. [10]
Deoxyribonuclease II (EC 3.1.22.1, DNase II, pancreatic DNase II, deoxyribonucleate 3'-nucleotidohydrolase, pancreatic DNase II, acid deoxyribonuclease, acid DNase) is an endonuclease that hydrolyzes phosphodiester linkages of deoxyribonucleotide in native and denatured DNA, yielding products with 3'-phosphates and 5'-hydroxyl ends, which occurs as a result of single-strand cleaving mechanism. [1]
Deoxyribonuclease I (usually called DNase I), is an endonuclease of the DNase family coded by the human gene DNASE1. [5] DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides.
Deoxyribonuclease IV (phage-T4-induced) (EC 3.1.21.2, endodeoxyribonuclease IV (phage T4-induced), E. coli endonuclease IV, endodeoxyribonuclease, redoxyendonuclease, deoxriboendonuclease, Escherichia coli endonuclease II, endonuclease II, DNA-adenine-transferase) is catalyzes the degradation nucleotides [1] in DsDNA by attacking the 5'-terminal end.
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13423 Ensembl ENSG00000105612 ENSMUSG00000003812 UniProt O00115 P56542 RefSeq (mRNA) NM_001375 NM_010062 NM_001368295 NM_001368296 RefSeq (protein) NP_001366 NP_001366.1 NP_034192 NP_001355224 NP_001355225 Location (UCSC) Chr 19: 12.88 – 12.88 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Deoxyribonuclease II, lysosomal is a protein that in humans is encoded by the DNASE2 ...